Zinc in PDB 7utt: Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination

All present enzymatic activity of Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination:
2.7.7.86;

The structure of Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination, PDB code: 7utt was solved by S.Wu, S.B.Gabelli, J.Sohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.67 / 2.04
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	77.093, 97.882, 142.271, 90, 90, 90
R / Rfree (%)	18.1 / 21

The structure of Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Zinc atom in the Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination (pdb code 7utt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination, PDB code: 7utt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:27.5 occ:1.00 NE2 A:HIS378 2.1 24.5 1.0 SG A:CYS385 2.3 29.0 1.0 SG A:CYS392 2.3 27.1 1.0 SG A:CYS384 2.3 26.9 1.0 CD2 A:HIS378 3.0 25.1 1.0 CE1 A:HIS378 3.1 27.1 1.0 CB A:CYS392 3.3 28.5 1.0 CB A:CYS385 3.4 27.7 1.0 CB A:CYS384 3.5 25.3 1.0 C A:CYS384 3.7 26.7 1.0 N A:CYS385 3.7 26.2 1.0 N A:CYS392 3.8 30.1 1.0 O A:HOH796 4.1 29.0 1.0 CA A:CYS392 4.1 29.3 1.0 O A:CYS384 4.1 25.6 1.0 CA A:CYS385 4.1 26.2 1.0 CA A:CYS384 4.1 24.3 1.0 CG A:HIS378 4.2 25.6 1.0 ND1 A:HIS378 4.2 24.9 1.0 NH1 A:ARG394 4.4 24.0 1.0 O A:HOH775 4.6 31.5 1.0 O A:HOH827 4.6 38.1 1.0 C A:CYS392 4.7 28.7 1.0 O A:CYS392 4.8 28.0 1.0 O A:HOH802 4.8 34.4 1.0 O A:ALA390 4.8 30.2 1.0 C A:LYS391 4.9 29.8 1.0

Zinc binding site 2 out of 2 in the Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn602 b:29.0 occ:1.00 NE2 C:HIS378 2.0 32.2 1.0 SG C:CYS384 2.3 29.6 1.0 SG C:CYS385 2.3 31.7 1.0 SG C:CYS392 2.4 29.1 1.0 CD2 C:HIS378 3.0 28.7 1.0 CE1 C:HIS378 3.1 32.1 1.0 CB C:CYS392 3.3 30.8 1.0 CB C:CYS385 3.4 28.7 1.0 CB C:CYS384 3.5 26.6 1.0 N C:CYS385 3.7 28.1 1.0 C C:CYS384 3.7 28.7 1.0 N C:CYS392 3.8 31.6 1.0 CA C:CYS385 4.1 28.4 1.0 CA C:CYS392 4.1 30.7 1.0 CA C:CYS384 4.1 26.9 1.0 O C:CYS384 4.1 26.7 1.0 CG C:HIS378 4.2 27.4 1.0 ND1 C:HIS378 4.2 26.9 1.0 O C:HOH769 4.3 35.1 1.0 NH1 C:ARG394 4.3 26.1 1.0 O C:HOH787 4.5 42.9 1.0 O C:HOH736 4.6 36.1 1.0 C C:CYS392 4.7 28.3 1.0 O C:ALA390 4.7 31.1 1.0 O C:HOH758 4.7 33.8 1.0 O C:CYS392 4.8 29.4 1.0 C C:LYS391 4.9 34.5 1.0

S.Wu, S.B.Gabelli, J.S.Sohn. Structure of Non-Hydrolyzable Atp (Apcpp) Binds to Cyclic Gmp Amp Synthase (Cgas) Through Mn Coordination To Be Published.